The findings of the study call into question a long-held belief about the way proteins fold within our cells and have significant ramifications for the treatment of illnesses connected to protein misfolding. A groundbreaking study by researchers at the Department of Energy's SLAC National Acceler
has uncovered the process by which a small cellular machine called TRiC controls the folding of tubulin, a human protein that is the foundation of microtubules, which act as the structural support and transportation system of cells.
This animation gives a 3D view of a finished, folded tubulin molecule that’s still attached to two subunits of a cellular machine called TRiC. A landmark study by researchers at SLAC and Stanford revealed that the inner walls of the TRiC chamber actively direct the folding of TRiC into its final, active form. Credit: Yanyan Zhao/Stanford University.
The researchers captured four distinct steps in the TRiC-directed folding process at near-atomic resolution with cryo-EM and confirmed what they saw with biochemical and biophysical analyses. The TRiC chamber is unique in that it consists of eight different subunits that form two stacked rings. A long, skinny strand of tubulin protein is delivered into the opening of the chamber by a helper molecule shaped like a jellyfish. Then the chamber’s lid closes and folding begins. When it’s done, the lid opens and the finished folded tubulin leaves.
The scientists discovered that the inside of this unique chamber directs the folding process in two ways.
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